title: Diversity in protein glycosylation among insect species.
abstract: BACKGROUND
  A very common protein modification in multicellular organisms is protein glycosylation or the addition of carbohydrate structures to the peptide backbone. Although the Class of the Insecta is the largest animal taxon on Earth, almost all information concerning glycosylation in insects is derived from studies with only one species, namely the fruit fly Drosophila melanogaster.
  
  
  RESULTS
  In this report, the differences in glycoproteomes between insects belonging to several economically important insect orders were studied. Using GNA (Galanthus nivalis agglutinin) affinity chromatography, different sets of glycoproteins with mannosyl-containing glycan structures were purified from the flour beetle (Tribolium castaneum), the silkworm (Bombyx mori), the honeybee (Apis mellifera), the fruit fly (D. melanogaster) and the pea aphid (Acyrthosiphon pisum). To identify and characterize the purified glycoproteins, LC-MS/MS analysis was performed. For all insect species, it was demonstrated that glycoproteins were related to a broad range of biological processes and molecular functions. Moreover, the majority of glycoproteins retained on the GNA column were unique to one particular insect species and only a few glycoproteins were present in the five different glycoprotein sets. Furthermore, these data support the hypothesis that insect glycoproteins can be decorated with mannosylated O-glycans.
  
  
  CONCLUSIONS
  The results presented here demonstrate that oligomannose N-glycosylation events are highly specific depending on the insect species. In addition, we also demonstrated that protein O-mannosylation in insect species may occur more frequently than currently believed.
authors.affiliation: Laboratory of Agrozoology, Department of Crop Protection, Faculty of Bioscience Engineering, Ghent University, Ghent, Belgium.
authors.forename: Gianni
authors.initials: G
authors.lastname: Vandenborre
authors.forename: Guy
authors.initials: G
authors.lastname: Smagghe
authors.forename: Bart
authors.initials: B
authors.lastname: Ghesquière
authors.forename: Gerben
authors.initials: G
authors.lastname: Menschaert
authors.forename: Rameshwaram
authors.initials: R
authors.lastname: Nagender Rao
authors.forename: Kris
authors.initials: K
authors.lastname: Gevaert
authors.forename: Els J M
authors.initials: EJ
authors.lastname: Van Damme
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001516:Bees / Q000737:chemistry / Q000378:metabolism; D002846:Chromatography, Affinity; D004331:Drosophila melanogaster / Q000737:chemistry / Q000378:metabolism; D006023:Glycoproteins / Q000032:analysis / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D006031:Glycosylation; D019476:Insect Proteins / Q000032:analysis / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D007313:Insecta / Q000378:metabolism*; D037241:Mannose-Binding Lectins / Q000378:metabolism; D055442:Metabolome; D008969:Molecular Sequence Data; D010802:Phylogeny; D037121:Plant Lectins / Q000378:metabolism; D011485:Protein Binding; D011499:Protein Processing, Post-Translational / Q000502:physiology; D013045:Species Specificity; D014231:Tribolium / Q000737:chemistry / Q000378:metabolism
chemical_list: D006023:Glycoproteins; D019476:Insect Proteins; D037241:Mannose-Binding Lectins; D037121:Plant Lectins; C063117:snowdrop lectin